Combining natural sequence variation with high throughput mutational data to reveal protein interaction sites.

ABSTRACT: Many protein interactions are conserved among organisms despite changes in the amino acid sequences that comprise their contact sites, a property that has been used to infer the location of these sites from protein homology. In an inter-species complementation experiment, a sequence present in a homologue is substituted into a protein and tested for its ability to support function. Therefore, substitutions that inhibit function can identify interaction sites that changed over evolution. However, most of the sequence differences within a protein family remain unexplored because of the small-scale nature of these complementation approaches. Here we use existing high throughput mutational data on the in vivo function of the RRM2 domain of the Saccharomyces cerevisiae poly(A)-binding protein,

SUBMITTER: Melamed D 

PROVIDER: S-EPMC4335499 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature